Evidence map›Paper›PMID 9632819›Full record

ArticleMolecular and cellular biology1998

Targeting to transcriptionally active loci by the hydrophilic N-terminal domain of Drosophila DNA topoisomerase I.

W L Shaiu, T S Hsieh

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. DNA and RNA topoisomerase activities of Top3β are promoted by mediator protein Tudor domain-containing protein 3.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The phosphoCTD-interacting domain of Topoisomerase I.Biochemical and biophysical research communications · 2010
    Article
  12. Article
  13. Article
  14. Article
  15. Preferential cleavage of plasmid-based R-loops and D-loops by Drosophila topoisomerase IIIbeta.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  16. Cellular roles of DNA topoisomerases: a molecular perspective.Nature reviews. Molecular cell biology · 2002
    Review
  17. Subnuclear distribution of topoisomerase I is linked to ongoing transcription and p53 status.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  18. Article
  19. Transcriptional consequences of topoisomerase inhibition.Molecular and cellular biology · 2001
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

W L ShaiuDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
T S Hsieh
Duke University Hospital · US

Funding

FUNCTION AND MECHANISM OF DNA TOPOISOMERASER01GM029006 · NIGMS · DUKE UNIVERSITY · PI HSIEH, TAO-SHIH · 1985 to 2010
$5.5M
NIGMS NIH HHS GM29006NIGMS NIH HHS R01 GM029006
6 · The paper itself

Abstract

DNA topoisomerase I (topo I) from Drosophila melanogaster contains a nonconserved, hydrophilic N-terminal domain of about 430 residues upstream of the conserved core domains. Deletion of this N terminus did not affect the catalytic activity of topo I, while further removal of sequences into the conserved regions inactivated its enzymatic activity. We have investigated the cellular function of the Drosophila topo I N-terminal domain with top1-lacZ transgenes. There was at least one putative nuclear localization signal within the first 315 residues of the N-terminal domain that allows efficient import of the large chimeric proteins into Drosophila nuclei. The top1-lacZ fusion proteins colocalized with RNA polymerase II (pol II) at developmental puffs on the polytene chromosomes. Either topo I or the top1-lacZ fusion protein was colocalized with RNA pol II in some but not all of the nonpuff, interband loci. However, the fusion proteins as well as RNA pol II were recruited to heat shock puffs during heat treatment, and they returned to the developmental puffs after recovery from heat shock. By immunoprecipitation, we showed that two of the largest subunits of RNA pol II coprecipitated with the N-terminal 315-residue fusion protein by using antibodies against beta-galactosidase. These data suggest that the topo I fusion protein can be localized to the transcriptional complex on chromatin and that the N-terminal 315 residues were sufficient to respond to cellular processes, especially during the reprogramming of gene expression.

Indexed as

Transcriptional ActivationAnimalsBinding SitesChromosomesDNA Topoisomerases, Type IDrosophila melanogasterHeat-Shock ResponseLac OperonNuclear Localization SignalsPrecipitin TestsRabbitsRecombinant Fusion ProteinsTime FactorsDNA Topoisomerases, Type INuclear Localization SignalsRecombinant Fusion Proteins

Identifiers

PMID9632819
PMCPMC109019
OpenAlexW2156345348

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.